Research workbench
Crystal structure of human atic in complex with folate- based inhibitor, BW2315U89UC
Analyse Crystal structure of human atic in complex with folate- based inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PL0
- Type
- protein
- Length
- 2,340 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional purine biosynthesis protein purh
- EC
- 2.1.2.3, 3.5.4.10
- UniProt
- P31939
- Ligands
- AMZ, XMP, BW2, K
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh (EC 2.1.2.3, 3.5.4.10) | protein | 589 | 42% helix, 19% strand | P31939 |
| B | Bifunctional purine biosynthesis protein purh (EC 2.1.2.3, 3.5.4.10) | protein | 587 | 41% helix, 18% strand | P31939 |
| C | Bifunctional purine biosynthesis protein purh (EC 2.1.2.3, 3.5.4.10) | protein | 585 | 42% helix, 19% strand | P31939 |
| D | Bifunctional purine biosynthesis protein purh (EC 2.1.2.3, 3.5.4.10) | protein | 579 | 41% helix, 18% strand | P31939 |
Ligands and binding sites
- AMZ · Aminoimidazole 4-carboxamide ribonucleotide · ligand · 3 copies · chains A, B, C, D
- XMP · Xanthosine-5'-monophosphate · ligand · 2 copies · chains A, B, C, D
- BW2 · N-(4-{[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)amino]sulfonyl}benzoyl)glutamic acid · ligand · 2 copies · chains A, B, C, D
- K · Potassium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.83 | 0.96 | 43 | empty |
| 2 | 658 | 0.82 | 0.86 | 88 | empty |
| 3 | 1085 | 0.78 | 0.80 | 100 | AMZ |
| 4 | 442 | 0.78 | 0.86 | 59 | AMZ, BW2 |
| 5 | 107 | 0.78 | 0.98 | 24 | empty |
Interfaces
4 interfaces between chains.
- A–B · 6193 Ų buried · 89 hydrogen bonds · protein-protein
- C–D · 6023 Ų buried · 82 hydrogen bonds · protein-protein
- A–C · 133 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 30 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1PL0 · Crystal structure of human ATIC in complex with folate-based inhibitor, BW2315U89UC · the same entry in another collection · chain D against D, TM-score 1.00
- P31939 · AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein atic… · a predicted model of the same protein · chain C against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P31939
- Elsewhere: RCSB PDB 1PL0 · PDBe 1PL0 · UniProt P31939
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